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Information on EC 2.4.1.41 - polypeptide N-acetylgalactosaminyltransferase and Organism(s) Homo sapiens and UniProt Accession Q14435
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2.4.1.41 polypeptide N-acetylgalactosaminyltransferaseIUBMB Comments
Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass.
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Word Map
- 2.4.1.41
-
o-glycosylation
-
mucin-type
- mucin
- glycosyltransferase
- o-glycans
-
o-linked
- threonine
- gangliosides
- lectin
- calcinosis
- oligosaccharide
- metastasis
- calcification
-
hyperphosphatemic
- gm2
-
galactosyltransferase
- glycolipids
-
1,25-dihydroxyvitamin
-
phosphaturic
- gd1a
-
sialyltransferase
-
submaxillary
-
angptl3
-
mucin-like
- klotho
- hyperostosis
- muc5ac
-
factor-23
- apomucin
- analysis
- drug development
-
lutropin
-
asn-linked
- molecular biology
-
periarticular
- medicine
-
o-glycoproteins
- iga1
- villosa
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
+
=
+
Synonyms
galnt3, n-acetylgalactosaminyltransferase, galnt2, galnac-t3, galnac-t, galnt14, galnac-transferase, galnac transferase, galnac-t2, galnac-t1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
UDP-N-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase
-
(UDP)-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein
-
-
-
-
GalNAc-T
GalNAc-T1
GalNAc-T11
GalNAc-T14
GalNAc-T2
GalNAc-T3
GalNAc-T4
GalNAc-T6
GalNAc-transferase
glycoprotein acetylgalactosaminyltransferase
-
-
-
-
polypeptide N-acetylgalactosaminyltransferase
polypeptide N-acetylgalactosaminyltransferase 14
polypeptide-N-acetylgalactosamine transferase
-
-
-
-
ppGalNAc T2
ppGalNAc-T
ppGaNTase
-
-
-
-
protein-UDP acetylgalactosaminyltransferase
-
-
-
-
UDP GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase
-
-
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 18
member of Y subfamily (together with UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, 9 and 17)
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13V1
-
splice variant 1 of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13, a 198 bp intron between exons 10 and 11 is not spliced out resulting in alteration of the lectin domain
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 16
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 17
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 18
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 19
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 20
-
-
UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6
-
-
UDP-N-acetylgalactosamine polypeptide: N-acetylgalactosaminyl-transferase
-
UDP-N-acetylgalactosamine-glycoprotein N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine-protein N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:kappa-casein polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:polypeptide N-acetyl-alpha-galactosaminyltransferase
-
UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase
-
-
-
-
UDP-N-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase
-
uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
additional information
-
the enzyme belongs to the large family of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases, ppGalNAc Ts
GalNAc-T1
data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members
GalNAc-T2
data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members
GalNAc-transferase
-
-
-
-
ppGalNAc-T
-
-
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase
abbreviated as ppGalNAc T
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase
Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass.
CAS REGISTRY NUMBER
COMMENTARY
9075-15-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
5 UDP-N-acetyl-alpha-D-galactosamine + beta1-adrenergic receptor
5 UDP + (N-acetyl-alpha-D-galactosaminyl)5-beta1-adrenergic receptor
-
-
-
?
5 UDP-N-acetyl-D-galactosamine + DSTTPAPTTK
5 UDP + N-acetyl-D-galactosaminylated DSTTPAPTTK
IgA hinge-4GalNAc + UDP-GalNAc
IgA hinge-nGalNAc + UDP
-
-
-
?
MUC1-2GalNAc + UDP-GalNAc
MUC1-nGalNAc + UDP
-
-
-
?
MUC2-6GalNAc + UDP-GalNAc
MUC2-nGalNAc + UDP
-
-
-
?
MUC5AC + UDP-GalNAc
GalNAc-Thr9-MUC5AC + UDP
-
hT2CD, hT2: glycosylation site selection driven by and substrate binding through its catalytic domain, hT10: not catalysed by hT10 because hT10 does not recognize naked peptides
preferred site for glycosylation by hT2 and hT2CD compared to Thr-3, Thr-10 and Thr-13
-
?
MUC5AC glycopeptides + UDP-GalNAc
GalNAc-MUC5AC + UDP
-
hT2: site preference of glycosylation depends on location of pre-existing GalNAc and is mediated by its lectin domain which directs glycosylation 10 residues N- or C-terminal to an extant GalNAc residue and aids site selection only when potential site is N-terminal to an extant GalNAc residue not C-terminal, Thr-9 is no preferred site of glycosylation, hT10: must recognize existing GalNAc residues via its catalytic domain which directs selection to the glycosylation site immediately N-terminal to the present GalNAc,
-
-
?
MUC5AC-13 + UDP-GalNAc
GalNAc-Thr12-MUC5AC-13 + UDP
-
hT10, hT10CD, hT10CD-hT2LD
-
-
?
MUC5AC-13 + UDP-GalNAc
GalNAc-Thr3-MUC5AC-13 + UDP
-
hT2: substrate binding through its catalytic domain, hT10: transfer of only single GalNAc residues
predominant product of hT2 and hT10
-
?
MUC5AC-13 + UDP-GalNAc
GalNAc-Thr9-MUC5AC-13 + UDP
-
hT2, hT2CD: no initial burst phase during catalysis
not preferred by hT2, preferred by hT2CD
-
?
MUC5AC-3 + UDP-GalNAc
GalNAc-Thr13-MUC5AC-3 + UDP
-
hT2: no initial burst phase during catalysis, substrate binding through its catalytic domain, hT10: transfer of only single GalNAc residues
hT2: preferred site for glycosylation, mediated by enhanced product release through lectin domain, hT10: predominant product
-
?
MUC5AC-3 + UDP-GalNAc
GalNAc-Thr2-MUC5AC + UDP
-
hT10CD, hT10CD-hT2LD, hT10: catalysis faster than for MUCAC-9
-
-
?
MUC5AC-3 + UDP-GalNAc
GalNAc-Thr9-MUC5AC-3 + UDP
-
hT2, hT2CD
not preferred by hT2, hT2CD: preferred site for glycosylation, lack of lectin domain in hT2CD results in rate-limiting product release
-
?
MUC5AC-3,13 + UDP-GalNAc
GalNAc-Ser-5-MUC5AC-3,13 + UDP
-
hT2, not catalysed by hT2CD and hT2CD-hT10LD
preferred site by hT2
-
?
MUC5AC-3,13 + UDP-GalNAc
GalNAc-Thr2,12-MUC5AC-3,13 + UDP
-
hT10, hT10CD, hT10CD-hT2LD
-
-
?
MUC5AC-9 + UDP-GalNAc
GalNAc-Thr2-MUC5AC-9 + UDP
-
not catalysed by hT10CD and hT10CD-hT2LD, hT10: catalysis slower than for MUC5AC-3
preferred site of glycosylation by hT10
-
?
OSM fragment + UDP-Gal
OSM fragment-nGalNAc + UDP
-
-
-
?
UDP-GalNAc + EA2
GalNAc-EA2 + UDP
ternary complex of ppGalNAcT-2 in crystal structure PDB: 2FFU, UDP-GalNAc binding results in the closed confirmation of loop B which stabilises loop A by binding of loop A (N102) to loop B (R362), EA2 peptide binds in an extended confirmation
binary complex of UDP and ppGalNAcT-2 in crystal structure PDB: 2FFV
-
?
UDP-GalNAc + GAGA(X)5T(X)5AGAGK
UDP + GAGA(X)5(GalNAc)T(X)5AGAGK
very high correlation between peptide preferences of ppGalNAc T2 and fly orthologue PGANT2 with r(square) = 0.92
-
-
?
UDP-GalNAc + GAGA(X)nT(X)nAGAGK
GAGA(X)n(GalNAc)T(X)nAGAGK + UDP
library of unmodified peptides, with randomized residue at position X and n=3 or n=5, random peptide preferences are not significantly altered by increased peptide substrate length n=5 compared to n=3 or the proximity of flanking Gly and Ala residues to the site of glycosylation, major peptide substrate preference determinants are the 2 to 3 residues flanking the site of glycosylation
-
-
?
UDP-N-((2S)-2-azidopropanoyl)-alpha-D-galactosamine + peptide EA2-biotin
UDP + N-((2S)-2-azidopropanoyl)-alpha-D-galactosaminyl-peptide EA2-biotin
i.e. PTTDSTTPAPTTKK-biotin
-
-
-
UDP-N-acetyl-alpha-D-galactosamine + (glycosylated GTTPSPVPTTSTTSAP)
UDP + ?
-
natural-type (alpha-GalNAc-O-Thr) and unnatural-type (beta-GalNAc-O-Thr, alpha-Fuc-O-Thr and beta-GlcNAc-O-Thr) glycosylated
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Ac-CIRIQRGPGRAFVTIGKIGNMR
UDP + ?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + delta-opioid receptor
UDP + N-acetyl-alpha-D-galactosaminyl-delta-opioid receptor
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + GT[GalNAc]TPSPVPTTSTTSAP
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
-
-
glycosylation at Thr-3 and Thr-13
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + GT[GalNAc]TP[GalNAc]SPVPTTSTTSAP
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTST[GalNAc]TSAP
UDP + GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTST[GalNAc]TSAP
UDP + GT[GalNAc]TP[GalNAc]SPVPTTST[GalNAc]TSAP
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GT[GalNAc]TPSPVPTTSTTSAP
UDP + GT[GalNAc]TPSPVPTTS[GalNAc]T[GalNAc]TSAP
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GT[GalNAc]TPSPVPTTSTTSAP
UDP + G[GalNAc]T[GalNAc]TPSPVPTTST[GalNAc]TSAP
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
UDP + GT[GalNAc]TPSPVPTTS[GalNAc]T[GalNAc]TSAP
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + peptide EA2-biotin
UDP + N-acetyl-alpha-D-galactosaminyl-peptide EA2-biotin
i.e. PTTDSTTPAPTTKK-biotin
-
-
-
UDP-N-acetyl-alpha-D-galactosamine + polypeptide
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide angiopoietin-like 3
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide angiopoietin-like 3
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide EA2
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide EA2
sequence PTTDSTTPAPTTK
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide FGF23
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide FGF23
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPIV
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPIV
-
preferred substrate for isoforms ppGalNAc T2, T5, T13, T14, and T16
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPIV-C
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPIV-C
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPV
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPV
-
preferred substrate for isoforms ppGalNAc T3, T5, T6, T13, and T16
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide GPV-C
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide GPV-C
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide Muc1
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide Muc1
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide MUC13
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide MUC13
-
isoform GALNT14 contributes to the glycosylation of peptide MUC13, which is significantly higher in ovarian cancer cells compared with the normal/benign ovary tissues
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-CIRIQRGPGRAFVTIGKIGNMR
UDP + N-acetyl-D-galactosaminylated Ac-CIRIQRGPGRAFVTIGKIGNMR
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-PFVTHPGYD
UDP + N-acetyl-D-galactosaminylated Ac-PFVTHPGYD
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-QATEYEYLDYDFLPETEPPEM
UDP + N-acetyl-D-galactosaminylated Ac-QATEYEYLDYDFLPETEPPEM
UDP-N-acetyl-D-galactosamine + AHGVTSAPDTR
UDP + N-acetyl-D-galactosaminylated AHGVTSAPDTR
-
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
acceptor: apomucin motif encoded by the MUC5AC gene
-
-
?
UDP-N-acetyl-D-galactosamine + CPPTPSATTPAPPSSSAPPETTAA
UDP + N-acetyl-D-galactosaminylated CPPTPSATTPAPPSSSAPPETTAA
UDP-N-acetyl-D-galactosamine + fibronectin
UDP + N-acetyl-D-galactosaminyl-fibronectin
-
fibronectin is a physiological substrate for GalNAc-T3
-
-
?
UDP-N-acetyl-D-galactosamine + GAGAPGPTPGPAGAGK
UDP + GAGAPGP-(N-acetyl-D-galactosaminylT)-PGPAGAGK
-
optimal isozyme ppGalNAc T2 peptide substrate
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSA
UDP + N-acetyl-D-galactosaminyl-[GTTPSPVPTTSTTSA]
i.e. Muc5Ac peptide, multiple possible binding sites for N-acetyl-D-galactosamine on the peptide
-
-
?
UDP-N-acetyl-D-galactosamine + HIV-V3 peptide
UDP + N-acetyl-D-galactosaminyl-HIV-V3 peptide
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
UDP-N-acetyl-D-galactosamine + immunoglobulin A1
UDP + N-acetyl-D-galactosaminyl-immunoglobulin A1
-
O-linked glycosylation of the human IgA1 hinge region by ppGalNAc-T2, synthetic IgA hinge peptide: ppGalNAc-T2 shows strongest activity and is able to transfer GalNAc to almost all possible glycosylation sites, other ppGalNAc-Ts show extremely weak activities
-
-
?
UDP-N-acetyl-D-galactosamine + osteopontin
UDP + N-acetyl-D-galactosaminyl-osteopontin
-
isozyme ppGalNAc T10 prefers previously glycosylated peptides as substrates, ppGalNAc T10 exhibits a single large preference for Ser/Thr-O-GalNAc at the +1, C-terminal, position relative to the Ser or Thr acceptor site
-
-
?
UDP-N-acetyl-D-galactosamine + PRFQDSSSSKAPPPSLPSPSRL
UDP + N-actetyl-D-galactosaminylated PRFQDSSSSKAPPPSLPSPSRL
-
-
-
?
UDP-N-acetyl-D-galactosamine + PRFQDSSSSKAPPPSLPSPSRLPG
UDP + N-acetyl-D-galactosaminylated PRFQDSSSSKAPPPSLPSPSRLPG
-
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPISTTMVTPTPTPTC
UDP + N-actetyl-D-galactosaminylated PTTTPISTTMVTPTPTPTC
-
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPISTTTMVTPTPTPTC
UDP + N-acetyl-D-galactosaminylated PTTTPISTTTMVTPTPTPTC
mucin derived substrate
-
-
?
UDP-N-acetyl-D-galactosamine + QATEYEYLDYDFLPEC
UDP + N-acetyl-D-galactosaminylated QATEYEYLDYDFLPEC
-
-
-
?
UDP-N-acetyl-D-galactosamine + RPAPGSTAPPA
UDP + N-acetyl-D-galactosaminylated RPAPGSTAPPA
-
-
-
?
UDP-N-acetyl-D-galactosamine + syndecan-3
UDP + N-acetyl-D-galactosaminyl-syndecan-3
syndecan-3 may be a natural substrate for GalNAc-T13
-
-
?
UDP-N-acetyl-D-galactosamine + TAPPAHGVTSAPDTRPAPGSTAPP
UDP + N-acetyl-D-galactosaminylated TAPPAHGVTSAPDTRPAPGSTAPP
UDP-N-hex-5-ynoyl-alpha-D-galactosamine + peptide EA2-biotin
UDP + N-hex-5-ynoyl-alpha-D-galactosaminyl-peptide EA2-biotin
i.e. PTTDSTTPAPTTKK-biotin
-
-
-
5 UDP-N-acetyl-D-galactosamine + DSTTPAPTTK
5 UDP + N-acetyl-D-galactosaminylated DSTTPAPTTK
mucin derived substrate
-
-
?
5 UDP-N-acetyl-D-galactosamine + DSTTPAPTTK
5 UDP + N-acetyl-D-galactosaminylated DSTTPAPTTK
mucin derived substrate, acceptor substrate
-
-
?
erythropoietin T + UDP-Gal
erythropoietin T-nGalNAc + UDP
-
-
-
?
erythropoietin T + UDP-Gal
erythropoietin T-nGalNAc + UDP
also catalysed by mutants GalTNAc-T2-D458H and GalTNAc-T2-D541A
-
-
?
IgA hinge + UDP-GalNAc
IgA hinge-nGalNAc + UDP
-
-
-
?
IgA hinge + UDP-GalNAc
IgA hinge-nGalNAc + UDP
GalTNAc-T11 incorporates only two GalNAc residues into IgA hinge peptide
-
-
?
IgA hinge + UDP-GalNAc
IgA hinge-nGalNAc + UDP
mutant GalNAc-T2-D458H incorporates 1-2 fewer GalNAc residues than wild-type
-
-
?
MUC1 + UDP-GalNAc
MUC1-nGalNAc + UDP
GalNAc-T4 lectin domain does not exhibit selective specificities for peptide sequences, or the density or pattern of GalNAc glycosylation, GalNAc-T4 lectin domain mediates GalNAc-glycopeptide substrate specificity
-
-
?
MUC1 + UDP-GalNAc
MUC1-nGalNAc + UDP
mutant GalNAc-T2-D458H incorporates 1-2 fewer GalNAc residues than wild-type, GalNAc-T2 lectin domain does not exhibit selective specificities for peptide sequences, or the density or pattern of GalNAc glycosylation
-
-
?
UDP-galactose + Muc1 peptide
UDP + galactosyl-Muc1 peptide
-
synthetic substrate
-
?
UDP-galactose + Muc1 peptide
UDP + galactosyl-Muc1 peptide
-
2 of 3 threonine residues on the Muc1 tandem repeat peptides, none of the serine residues, maximum is 2 Mol of GalNAc linked to each 20-residue repeat unit
-
?
UDP-galactose + Muc2 peptide
UDP + galactosyl-Muc2 peptide
-
peptides derived of Muc2 mucin
-
-
?
UDP-galactose + Muc2 peptide
UDP + galactosyl-Muc2 peptide
-
only GalNAc-T2, only with the Muc2 acceptor peptide
-
-
?
UDP-galactose + Muc2 peptide
UDP + galactosyl-Muc2 peptide
-
investigation of preferences for distinct threonine residues in the peptide sequences
-
-
?
UDP-galactose + PTTTPITTTTK
UDP + galactosyl-PTTTPITTTTK
-
Muc2 peptide, investigation of preferences for distinct threonine residues in the peptide sequences of isozyme T1 to T4
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-QATEYEYLDYDFLPETEPPEM
UDP + N-acetyl-D-galactosaminylated Ac-QATEYEYLDYDFLPETEPPEM
-
-
-
?
UDP-N-acetyl-D-galactosamine + Ac-QATEYEYLDYDFLPETEPPEM
UDP + N-acetyl-D-galactosaminylated Ac-QATEYEYLDYDFLPETEPPEM
acceptor substrate
-
-
?
UDP-N-acetyl-D-galactosamine + AHGVVTSAPDTR
UDP + ?
i.e. Muc1, 3% of the activity with Muc5AC as substrate, enzyme form pp-GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + AHGVVTSAPDTR
UDP + ?
i.e. Muc1a, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + ANTPSFPTATSPAPPI
UDP + ?
i.e. Muc13, about 25% of the activity with Muc5AC as substrate, enzyme form pp-GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + ANTPSFPTATSPAPPI
UDP + ?
i.e. Muc13, about 50% of the activity with Muc1a, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + CPPTPSATTPAPPSSSAPPETTAA
UDP + N-acetyl-D-galactosaminylated CPPTPSATTPAPPSSSAPPETTAA
mucin derived substrate
-
-
?
UDP-N-acetyl-D-galactosamine + CPPTPSATTPAPPSSSAPPETTAA
UDP + N-acetyl-D-galactosaminylated CPPTPSATTPAPPSSSAPPETTAA
mucin derived substrate, acceptor substrate
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
GalNAc-T7: exclusive specificity for partially GalNAc-glycosylated acceptor substrates, GalNAc-glycosylated peptide substrates derived from the tandem repeats of human Muc2 and rat submandibular gland mucin, specificity of GalNAc-T4
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
rGalNAc-T4 is dependent on the presence of GalNAc on acceptor peptides, activity is triggered by a lectin-like interaction of enzyme with the glycopeptide directed by the putative lectin domain found in the C-terminal region, rGalNAc-T2 activity is enhanced on glycosylated acceptor peptides
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
ppGalNAc-T14 can utilize GalNAc transferred peptides as substrates
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
ppGalNAc-T4 and -T7 prefer peptides having GalNAc residues as acceptor substrates
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
acceptors: partially glycosylated versions of a peptide derived from mucin2, pp-GalNAc-T1, -T2, -T3 and -T4 exhibit distinct specificities toward glycopeptides, pathway of incorporation of the second and third GalNAc, isoenzymes may recognize directly GalNAc residues in the vicinity
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAk
UDP + ?
i.e. Muc5AC, about 55% of the activity with Muc1a, pp-GalNAc-T15 shows significantly less catalytic activity than pp-GalNAc-T2,T15 transferrs up to seven GalNAcs to the Muc5AC peptide, while T2 transferrs up to five GalNAcs, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAk
UDP + ?
i.e. Muc5AC, pp-GalNAc-T15 shows significantly less catalytic activity than pp-GalNAc-T2,T15 transferrs up to seven GalNAcs to the Muc5AC peptide, while T2 transferrs up to five GalNAcs
-
-
?
UDP-N-acetyl-D-galactosamine + HIV-V3 peptide
UDP + N-acetyl-D-galactosaminyl-HIV-V3 peptide
-
HIVIIIBgp120, only GalNAc-T3
-
-
?
UDP-N-acetyl-D-galactosamine + HIV-V3 peptide
UDP + N-acetyl-D-galactosaminyl-HIV-V3 peptide
-
placenta, but not liver enzyme
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
-
placenta enzyme
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
-
only Ser acceptor sites, with a very low activity
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
-
only GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
ppGalNAc-T14: acceptors are mucin-derived peptides such as Muc2, Muc5AC, Muc7, Muc13
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
ppGalNAc-T13: acceptors are mucin peptides, such as Muc1a', Muc5Ac and Muc7, forms a triplet Tn epitope, 3 consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, different substrate specificities of ppGalNAc-T1 and -T13
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
substrate specificities of recombinant ppGalNAc-T1, -T2, -T3, -T4, -T6 and T9
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
site-specific O-glycosylation by rGalNAc-T2 and -T4 is controlled by the primary sequence context and the position and structure of previously introduced O-glycans, acceptors: synthetic mucin-type peptides and glycopeptides derived from tandem repeat regions of MUC1, MUC2 and MUC4, minimum peptide length is required, which is larger for glycosylated substrates, concerted and sequential action of rGalNAc-T2 and -T4 fully glycosylates MUC1, but only partially MUC2 and MUC4 tandem repeat peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptor specificity
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
GalNAc-T1 and -T3: strict specificity for UDP-GalNAc, GalNAc-T2: utilizes UDP-GalNAc and UDP-Gal
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptor: mucin2 derived fluorescein-conjugated peptide Pro-Thr-Thr-Thr-Pro-Leu-Lys, preferential sites of O-glycosylation by pp-GalNAc-T1, -T2, -T3 and -T4, of which each has a unique specificity
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptor: human MUC5AC peptide Thr-Thr-Ser-Ala-Pro-Thr-Thr-Ser
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: human mucin Muc1 and Muc2 peptides, human chorionic gonadotropin-beta peptide, HIV-V3 peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
3 GalNAc-transferases: GalNAc-T1, -T2 and -T3 with distinct but partly overlapping specificities, dependent on the primary sequence of the acceptor substrate, acceptors: peptides based on Muc1 tandem repeat, TAP24, Muc2, Muc5AC, erythropoietin, hCG-beta, HIVIIIBgp120, ovine submaxillary mucin fragment, peptide derived from fibronectin, GalNAc-T1, -T2 and -T3 react at different rates with individual sites in the Muc1 repeat
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
ppGalNAc-T13: synthesis of O-glycan, specifically the Tn antigen in neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
GalNAc-T7: functions as a follow-up enzyme in the initiation step of O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
different enzyme activities are involved in the initiation of GalNAc O-glycosylation and these are differentially expressed in cells and organs
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
ppGalNAc-T14 may be involved in O-glycosylation in kidney
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
GalNAc-T9 catalyzes O-glycosylation in brain
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
post-translational, initial reaction in O-linked oligosaccharide biosynthesis
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
ppGalNAc-T2: initiation of O-glycosylation in the IgA1 hinge region
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
usage of random peptide substrates, overview. Isozyme substrate specificities, amino acid residue enhancement factors for ppGalNAc T isozymes are obtained from random peptide substrates, detailed overview
product analysis by NMR and mass spectrometry
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTT
UDP + ?
i.e. EA2, about 25% of the activity with Muc1a, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTT
UDP + ?
i.e. EA2, about 35% of the activity with Muc5AC as substrate, enzyme form pp-GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPITTTTTVTPTPTPTGTQT
UDP + ?
i.e. Muc2, about 35% of the activity with Muc1a, enzyme form pp-GalNAc-T15
-
-
?
UDP-N-acetyl-D-galactosamine + PTTTPITTTTTVTPTPTPTGTQT
UDP + ?
i.e. Muc2, about 95% of the activity with Muc5AC as substrate, enzyme form pp-GalNAc-T2
-
-
?
UDP-N-acetyl-D-galactosamine + TAPPAHGVTSAPDTRPAPGSTAPP
UDP + N-acetyl-D-galactosaminylated TAPPAHGVTSAPDTRPAPGSTAPP
-
-
-
?
UDP-N-acetyl-D-galactosamine + TAPPAHGVTSAPDTRPAPGSTAPP
UDP + N-acetyl-D-galactosaminylated TAPPAHGVTSAPDTRPAPGSTAPP
acceptor substrate
-
-
?
additional information
?
-
GalNAc-T7: no activity with non-glycosylated peptides and GalNAc-glycosylated Muc1 substrate
-
-
?
additional information
?
-
-
GalNAc-T7: no activity with non-glycosylated peptides and GalNAc-glycosylated Muc1 substrate
-
-
?
additional information
?
-
-
different substrate specificities before and after Muc2 affinity chromatography of enzyme
-
-
?
additional information
?
-
-
14 distinct isoforms different with regard to their expression and specificity, but overlaps also occur, ppGalNAc-T14 forms together with ppGalNAc-T2 a subfamily of ppGalNAc-T gene family
-
-
?
additional information
?
-
-
all known rGalNAc-Ts are characterized by a putative lectin domain in their C-terminal regions
-
-
?
additional information
?
-
-
GalNAc-T9 contains a 485-amino acid putative catalytic region, GalNAc-T1, -T2, -T4 and -T8 belongs to the housekeeping enzymes with ubiquitous expression, GalNAc-T3, -T5, -T6, -T7 and -T9 belongs to the tissue-specific enzymes
-
-
?
additional information
?
-
-
existence of multiple enzyme activities, differentially expressed in different organs, at least 2 distinct enzyme specificities
-
-
?
additional information
?
-
-
amino acid sequences of seven GalNAc-transferases
-
-
?
additional information
?
-
amino acid sequences of seven GalNAc-transferases
-
-
?
additional information
?
-
-
amino acid sequences of seven GalNAc-transferases
-
-
?
additional information
?
-
-
pp-GalNAc-T13 is specifically expressed in neurons and synthesizes Tn antigen
-
-
?
additional information
?
-
pp-GalNAc-T13 is specifically expressed in neurons and synthesizes Tn antigen
-
-
?
additional information
?
-
MUC1-2GalNAc, MUC2-6GalNAc, OSM fragments, hCG-beta are not substrates for GalNAc-T11
-
-
?
additional information
?
-
MUC1-2GalNAc, MUC2-6GalNAc, OSM fragments, hCG-beta are not substrates for GalNAc-T11
-
-
?
additional information
?
-
MUC1-2GalNAc, MUC2-6GalNAc, OSM fragments, hCG-beta are not substrates for GalNAc-T11
-
-
?
additional information
?
-
MUC1-2GalNAc, MUC2-6GalNAc, OSM fragments, hCG-beta are not substrates for GalNAc-T11
-
-
?
additional information
?
-
MUC1b' and hCG-beta are no substrates for GalNAc-T1
-
-
?
additional information
?
-
MUC1b' and hCG-beta are no substrates for GalNAc-T1
-
-
?
additional information
?
-
MUC1b' and hCG-beta are no substrates for GalNAc-T1
-
-
?
additional information
?
-
MUC1b' and hCG-beta are no substrates for GalNAc-T1
-
-
?
additional information
?
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases transfer GalNAc from UDP-GalNAc to the Ser and Thr residues of polypeptide acceptors, and initiate and regulate mucin-type O-glycosylation
-
-
?
additional information
?
-
-
most active with partially glycosylated MUC5AC (by a combination of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 and UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2)
-
-
?
additional information
?
-
-
no activity observed with substrate peptides of other UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases
-
-
?
additional information
?
-
no activity with 2'-deoxy-alpha-D-galactosamine or 2'-oxymethyl-alpha-D-galactosamine
-
-
?
additional information
?
-
-
no activity with 2'-deoxy-alpha-D-galactosamine or 2'-oxymethyl-alpha-D-galactosamine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide EA2
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide EA2
sequence PTTDSTTPAPTTK
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide Muc1
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide Muc1
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide MUC13
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide MUC13
-
isoform GALNT14 contributes to the glycosylation of peptide MUC13, which is significantly higher in ovarian cancer cells compared with the normal/benign ovary tissues
-
-
?
UDP-N-acetyl-D-galactosamine + fibronectin
UDP + N-acetyl-D-galactosaminyl-fibronectin
-
fibronectin is a physiological substrate for GalNAc-T3
-
-
?
UDP-N-acetyl-D-galactosamine + syndecan-3
UDP + N-acetyl-D-galactosaminyl-syndecan-3
syndecan-3 may be a natural substrate for GalNAc-T13
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
ppGalNAc-T13: synthesis of O-glycan, specifically the Tn antigen in neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
GalNAc-T7: functions as a follow-up enzyme in the initiation step of O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
different enzyme activities are involved in the initiation of GalNAc O-glycosylation and these are differentially expressed in cells and organs
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
ppGalNAc-T14 may be involved in O-glycosylation in kidney
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
GalNAc-T9 catalyzes O-glycosylation in brain
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
post-translational, initial reaction in O-linked oligosaccharide biosynthesis
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
ppGalNAc-T2: initiation of O-glycosylation in the IgA1 hinge region
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
additional information
?
-
-
pp-GalNAc-T13 is specifically expressed in neurons and synthesizes Tn antigen
-
-
?
additional information
?
-
pp-GalNAc-T13 is specifically expressed in neurons and synthesizes Tn antigen
-
-
?
additional information
?
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases transfer GalNAc from UDP-GalNAc to the Ser and Thr residues of polypeptide acceptors, and initiate and regulate mucin-type O-glycosylation
-
-
?
additional information
?
-
no activity with 2'-deoxy-alpha-D-galactosamine or 2'-oxymethyl-alpha-D-galactosamine
-
-
?
additional information
?
-
-
no activity with 2'-deoxy-alpha-D-galactosamine or 2'-oxymethyl-alpha-D-galactosamine
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
hydrated by a single water molecule in the presence of UDP-GalNAc or UDP-GalNAc and peptide
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fully GalNAc-substituted MUC1 repeat peptide
-
inhibits activity of rGalNAc-T4 and -T2
-
N-acetyl-alpha-D-galactosamine
-
the acetylated enzyme is strongly inhibited by N-acetyl-alpha-D-galactosamine
EDTA
inhibition of GalNAc-T2 enzyme and lectin domain
GalNAc
inhibition for GalNAc-T2 lectin domain to bind GalNAc-MUC1
GalNAc
inhibition for GalNAc-T4 lectin domain to bind GalNAc-MUC1
additional information
-
elongation of GalNAc by beta3-galactosylation inhibits rGalNAc-T4 activity completely and rGalNAc-T2 activity with respect to the acceptor site GSTA, not inhibited by GlcNAc
-
additional information
benzyl or phenyl alpha and beta-GalNAc compounds show higher inhibition for GalNAc-T2 to bind GalNAc-MUC1 than for isoform GalNAc-T4. No inhibition of GalNAc-T2 enzyme and lectin domain by glucose, GlcNAc or mannose
-
additional information
benzyl or phenyl alpha and beta-GalNAc compounds show higher inhibition for GalNAc-T2 to bind GalNAc-MUC1 than for isoform GalNAc-T4. No inhibition of GalNAc-T2 enzyme and lectin domain by glucose, GlcNAc or mannose
-
additional information
benzyl or phenyl alpha and beta-GalNAc compounds show higher inhibition for GalNAc-T2 to bind GalNAc-MUC1 than for isoform GalNAc-T4. No inhibition of GalNAc-T2 enzyme and lectin domain by glucose, GlcNAc or mannose
-
additional information
benzyl or phenyl alpha and beta-GalNAc compounds show higher inhibition for GalNAc-T2 to bind GalNAc-MUC1 than for isoform GalNAc-T4. No inhibition of GalNAc-T2 enzyme and lectin domain by glucose, GlcNAc or mannose
-
additional information
benzyl or phenyl alpha and beta-GalNAc compounds show weaker inhibition for GalNAc-T4 to bind GalNAc-MUC1 than for isoform GalNAc-T2. No inhibition of GalNAc-T4 enzyme and lectin domain by glucose, GlcNAc or mannose
-
additional information
benzyl or phenyl alpha and beta-GalNAc compounds show weaker inhibition for GalNAc-T4 to bind GalNAc-MUC1 than for isoform GalNAc-T2. No inhibition of GalNAc-T4 enzyme and lectin domain by glucose, GlcNAc or mannose
-
additional information
benzyl or phenyl alpha and beta-GalNAc compounds show weaker inhibition for GalNAc-T4 to bind GalNAc-MUC1 than for isoform GalNAc-T2. No inhibition of GalNAc-T4 enzyme and lectin domain by glucose, GlcNAc or mannose
-
additional information
benzyl or phenyl alpha and beta-GalNAc compounds show weaker inhibition for GalNAc-T4 to bind GalNAc-MUC1 than for isoform GalNAc-T2. No inhibition of GalNAc-T4 enzyme and lectin domain by glucose, GlcNAc or mannose
-
additional information
-
not inhibited by by D-glucose or UDP-N-acetyl-alpha-D-galactosamine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
GalNAc-T7: selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human Muc2 and rat submaxillary gland mucin
-
additional information
-
GalNAc-T7: selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human Muc2 and rat submaxillary gland mucin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.206
GT[GalNAc]TPSPVPTTST[GalNAc]TSAP
-
pH not specified in the publication, 37°C
0.043
UDP-N-((2S)-2-azidopropanoyl)-alpha-D-galactosamine
mutant 253A/L310A, pH 7.4, 37°C
0.0026
UDP-N-hex-5-ynoyl-alpha-D-galactosamine
mutant 253A/L310A, pH 7.4, 37°C
0.01
IgA hinge
+/-0.01 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.02
IgA hinge
+/-0.005 mM, mutant GalNAc-T2-D458H, pH7.4
-
0.32
IgA hinge-4GalNAc
+/-0.09 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.81
IgA hinge-4GalNAc
+/-0.2 mM, mutant GalNAc-T2-D458H, pH7.4
-
0.15
MUC1
+/-0.03 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.36
MUC1
+/-0.19mM, mutant GalNAc-T2-D458H, pH7.4
-
0.86
MUC1-2GalNAc
+/-0.21 mM, mutant GalNAc-T2-D541A, pH7.4
0.018
Muc2
+/-0.003 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.25
Muc2
+/-0.006 mM, mutant GalNAc-T2-D458H, pH7.4
-
0.066
MUC2-6GalNAc
+/-0.010 mM, mutant GalNAc-T2-D541A, pH7.4
-
0.036
UDP-Gal
+/-0.001 mM, mutant GalNAc-T2-D458H, pH7.4
0.041
UDP-Gal
+/-0.005 mM, mutant GalNAc-T2-D541A, pH7.4
0.013
UDP-GalNAc
+/-0.001 mM, mutant GalNAc-T2-D541A, pH7.4
0.03
UDP-GalNAc
+/-0.001 mM, mutant GalNAc-T2-D458H, pH7.4
0.16
UDP-GalNAc
determination of Km for UDP-GalNAc is performed with saturating concentration of CPPTPSATTPAPPSSSAPPETTAA as substrate. No incorporation is found with UDP-Gal or UDP-GlcNAc
0.016
UDP-N-acetyl-D-galactosamine
pH 7.4, 37°C, enzyme form pp-GalNAc-T15
0.081
UDP-N-acetyl-D-galactosamine
pH 7.4, 37°C, enzyme form pp-GalNAc-T2
additional information
additional information
-
values for different human mucin Muc1 peptides
-
additional information
additional information
-
values for GalNAc-T1, -T2 and -T3 for different substrate peptides
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.566
UDP-N-((2S)-2-azidopropanoyl)-alpha-D-galactosamine
mutant 253A/L310A, pH 7.4, 37°C
0.158
UDP-N-hex-5-ynoyl-alpha-D-galactosamine
mutant 253A/L310A, pH 7.4, 37°C
additional information
additional information
-
hT2 catalysed glycosylation of MUC5AC and MUC5AC-13 follows a biphasic time course: fast formation of enzyme-product (initial burst phase: 1 molecule product per molecule hT2 enzyme), slow and rate-limiting product release
-
additional information
additional information
-
hT2 catalysed glycosylation of MUC5AC-3 follows a linear time course: rate limiting catalysis or substrate binding
-
additional information
additional information
-
steady-state rates of hT2 catalysis are less than 1 reaction per second at room temperature
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
UDP-N-((2S)-2-azidopropanoyl)-alpha-D-galactosamine
mutant 253A/L310A, pH 7.4, 37°C
61
UDP-N-hex-5-ynoyl-alpha-D-galactosamine
mutant 253A/L310A, pH 7.4, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
benzyl N-acetyl-alpha-D-galactosamine
Homo sapiens
-
acetylated wild type enzyme, at pH 7.4 and 37°C
50
D-galactose
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
50
methyl-alpha-Gal
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
40
methyl-beta-Gal
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
8
ortho-nitrophenyl-beta-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
10
para-nitrophenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
1
benzyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
5
benzyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
15
benzyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2
20
benzyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
1
GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
5
GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
15
GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2
37
GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
20
N-acetyl-alpha-D-galactosamine
Homo sapiens
-
acetylated wild type enzyme, at pH 7.4 and 37°C
0.5
o-nitrophenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
5
o-nitrophenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
7
o-nitrophenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2
12
o-nitrophenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
1
o-nitrophenyl-beta-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
10
o-nitrophenyl-beta-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2
12
o-nitrophenyl-beta-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
1
p-nitrophenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
10
p-nitrophenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2
10
p-nitrophenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
0.8
p-nitrophenyl-beta-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
8
p-nitrophenyl-beta-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
10
p-nitrophenyl-beta-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2
10
p-nitrophenyl-beta-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
1
phenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
5
phenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2
5
phenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
15
phenyl-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2 lectin domain
30
UDP-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4
50
UDP-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T4 lectin domain
65
UDP-alpha-GalNAc
Homo sapiens
GalNAc-MUC1 binding to biotinylated GalNAc-T2
additional information
additional information
Homo sapiens
EDTA exhibits IC50 higher than 10 in all cases
-
additional information
additional information
Homo sapiens
EDTA exhibits IC50 higher than 10 in all cases
-
additional information
additional information
Homo sapiens
EDTA exhibits IC50 higher than 10 in all cases
-
additional information
additional information
Homo sapiens
EDTA exhibits IC50 higher than 10 in all cases
-
additional information
additional information
Homo sapiens
EDTA exhibits IC50s higher than 10 in all cases
-
additional information
additional information
Homo sapiens
EDTA exhibits IC50s higher than 10 in all cases
-
additional information
additional information
Homo sapiens
EDTA exhibits IC50s higher than 10 in all cases
-
additional information
additional information
Homo sapiens
EDTA exhibits IC50s higher than 10 in all cases
-
additional information
additional information
Homo sapiens
galactose and methyl-alpha/beta-Gal exhibit IC50 higher than 100 mM for GalNAc-T2 enzyme and lectin domain
-
additional information
additional information
Homo sapiens
galactose and methyl-alpha/beta-Gal exhibit IC50 higher than 100 mM for GalNAc-T2 enzyme and lectin domain
-
additional information
additional information
Homo sapiens
galactose and methyl-alpha/beta-Gal exhibit IC50 higher than 100 mM for GalNAc-T2 enzyme and lectin domain
-
additional information
additional information
Homo sapiens
galactose and methyl-alpha/beta-Gal exhibit IC50 higher than 100 mM for GalNAc-T2 enzyme and lectin domain
-
additional information
additional information
Homo sapiens
galactose and methyl-alpha/beta-Gal exhibit IC50s higher than 100 mM for GalNAc-T4 lectin domain
-
additional information
additional information
Homo sapiens
galactose and methyl-alpha/beta-Gal exhibit IC50s higher than 100 mM for GalNAc-T4 lectin domain
-
additional information
additional information
Homo sapiens
galactose and methyl-alpha/beta-Gal exhibit IC50s higher than 100 mM for GalNAc-T4 lectin domain
-
additional information
additional information
Homo sapiens
galactose and methyl-alpha/beta-Gal exhibit IC50s higher than 100 mM for GalNAc-T4 lectin domain
-
additional information
additional information
Homo sapiens
GalNAc-T2 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s
-
additional information
additional information
Homo sapiens
GalNAc-T2 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s
-
additional information
additional information
Homo sapiens
GalNAc-T2 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s
-
additional information
additional information
Homo sapiens
GalNAc-T2 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s
-
additional information
additional information
Homo sapiens
GalNAc-T4 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s
-
additional information
additional information
Homo sapiens
GalNAc-T4 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s
-
additional information
additional information
Homo sapiens
GalNAc-T4 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s
-
additional information
additional information
Homo sapiens
GalNAc-T4 lectin domain exhibits no specificity for anomeric configuration of GalNAc according to simlar IC50s
-
additional information
additional information
Homo sapiens
glucose derivatives, lactose and UDP exhibit IC50 higher than 100 mM in all cases
-
additional information
additional information
Homo sapiens
glucose derivatives, lactose and UDP exhibit IC50 higher than 100 mM in all cases
-
additional information
additional information
Homo sapiens
glucose derivatives, lactose and UDP exhibit IC50 higher than 100 mM in all cases
-
additional information
additional information
Homo sapiens
glucose derivatives, lactose and UDP exhibit IC50 higher than 100 mM in all cases
-
additional information
additional information
Homo sapiens
glucose derivatives, lactose and UDP exhibit IC50s higher than 100 mM in all cases
-
additional information
additional information
Homo sapiens
glucose derivatives, lactose and UDP exhibit IC50s higher than 100 mM in all cases
-
additional information
additional information
Homo sapiens
glucose derivatives, lactose and UDP exhibit IC50s higher than 100 mM in all cases
-
additional information
additional information
Homo sapiens
glucose derivatives, lactose and UDP exhibit IC50s higher than 100 mM in all cases
-
additional information
additional information
Homo sapiens
UDP exhibits similar inhibitory effects on GalNAc-T2 and mutant GalNAc-T2-D458H
-
additional information
additional information
Homo sapiens
UDP exhibits similar inhibitory effects on GalNAc-T2 and mutant GalNAc-T2-D458H
-
additional information
additional information
Homo sapiens
UDP exhibits similar inhibitory effects on GalNAc-T2 and mutant GalNAc-T2-D458H
-
additional information
additional information
Homo sapiens
UDP exhibits similar inhibitory effects on GalNAc-T2 and mutant GalNAc-T2-D458H
-
additional information
additional information
Homo sapiens
UDP-alpha-GalNAc exhibits IC50 higher than 100 mM for GalNAc-T2 lectin domain
-
additional information
additional information
Homo sapiens
UDP-alpha-GalNAc exhibits IC50 higher than 100 mM for GalNAc-T2 lectin domain
-
additional information
additional information
Homo sapiens
UDP-alpha-GalNAc exhibits IC50 higher than 100 mM for GalNAc-T2 lectin domain
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
118
+/-39, MUC1-2GalNAc by mutant GalNAc-T2-D541A, pH7.4
119
+/-24, IgA hinge-4GalNAc by mutant GalNAc-T2-D458H, pH7.4
145
+/-21, IgA hinge by mutant GalNAc-T2-D541A, pH7.4
236
+/-1, IgA hinge by mutant GalNAc-T2-D458H, pH7.4
292
+/-18, MUC2-6GalNAc by mutant GalNAc-T2-D541A, pH7.4
45
+/-13, UDP-GalNAc by mutant GalNAc-T2-D458H, pH7.4
46
+/-12, UDP-GalNAc by mutant GalNAc-T2-D541A, pH7.4
49
+/-5, IgA hinge-4GalNAc by mutant GalNAc-T2-D541A, pH7.4
additional information
additional information
0.005 +/-0.007 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D458H, pH7.4
additional information
0.005 +/-0.007 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D458H, pH7.4
additional information
0.005 +/-0.007 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D458H, pH7.4
additional information
0.005 +/-0.007 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D458H, pH7.4
additional information
0.025 +/-0.008 micromol/min/ml, MUC1-2GalNAC, pH7.4
additional information
0.025 +/-0.008 micromol/min/ml, MUC1-2GalNAC, pH7.4
additional information
0.025 +/-0.008 micromol/min/ml, MUC1-2GalNAC, pH7.4
additional information
0.025 +/-0.008 micromol/min/ml, MUC1-2GalNAC, pH7.4
additional information
0.028 +/-0.011 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D541A, pH7.4
additional information
0.028 +/-0.011 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D541A, pH7.4
additional information
0.028 +/-0.011 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D541A, pH7.4
additional information
0.028 +/-0.011 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D541A, pH7.4
additional information
0.029 +/-0.007 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D458H, pH7.4
additional information
0.029 +/-0.007 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D458H, pH7.4
additional information
0.029 +/-0.007 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D458H, pH7.4
additional information
0.029 +/-0.007 micromol/min/ml, MUC1-a' by mutant GalNAc-T2-D458H, pH7.4
additional information
0.039 +/-0.010 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.039 +/-0.010 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.039 +/-0.010 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.039 +/-0.010 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.046 +/-0.005 micromol/min/ml, MUC7 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.046 +/-0.005 micromol/min/ml, MUC7 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.046 +/-0.005 micromol/min/ml, MUC7 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.046 +/-0.005 micromol/min/ml, MUC7 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.046 +/-0.006 micromol/min/ml, MUC1-2GalNAC, pH7.4
additional information
0.046 +/-0.006 micromol/min/ml, MUC1-2GalNAC, pH7.4
additional information
0.046 +/-0.006 micromol/min/ml, MUC1-2GalNAC, pH7.4
additional information
0.046 +/-0.006 micromol/min/ml, MUC1-2GalNAC, pH7.4
additional information
0.046 +/-0.009 micromol/min/ml, MUC2-6GalNAc by mutant GalNAc-T2-D541A, pH7.4
additional information
0.046 +/-0.009 micromol/min/ml, MUC2-6GalNAc by mutant GalNAc-T2-D541A, pH7.4
additional information
0.046 +/-0.009 micromol/min/ml, MUC2-6GalNAc by mutant GalNAc-T2-D541A, pH7.4
additional information
0.046 +/-0.009 micromol/min/ml, MUC2-6GalNAc by mutant GalNAc-T2-D541A, pH7.4
additional information
0.047 +/-0.011 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D458H, pH7.4
additional information
0.047 +/-0.011 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D458H, pH7.4
additional information
0.047 +/-0.011 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D458H, pH7.4
additional information
0.047 +/-0.011 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D458H, pH7.4
additional information
0.053 +/-0.010 micromol/min/ml, MUC7 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.053 +/-0.010 micromol/min/ml, MUC7 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.053 +/-0.010 micromol/min/ml, MUC7 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.053 +/-0.010 micromol/min/ml, MUC7 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.054 +/-0.001 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D458H, pH7.4
additional information
0.054 +/-0.001 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D458H, pH7.4
additional information
0.054 +/-0.001 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D458H, pH7.4
additional information
0.054 +/-0.001 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D458H, pH7.4
additional information
0.055 +/-0.008 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D541A, pH7.4
additional information
0.055 +/-0.008 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D541A, pH7.4
additional information
0.055 +/-0.008 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D541A, pH7.4
additional information
0.055 +/-0.008 micromol/min/ml, MUC1-2GalNaC by mutant GalNAc-T2-D541A, pH7.4
additional information
0.062 +/-0.010 micromol/min/ml, MUC2-6GalNAc, pH7.4
additional information
0.062 +/-0.010 micromol/min/ml, MUC2-6GalNAc, pH7.4
additional information
0.062 +/-0.010 micromol/min/ml, MUC2-6GalNAc, pH7.4
additional information
0.062 +/-0.010 micromol/min/ml, MUC2-6GalNAc, pH7.4
additional information
0.065 +/-0.007 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D541A, pH7.4
additional information
0.065 +/-0.007 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D541A, pH7.4
additional information
0.065 +/-0.007 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D541A, pH7.4
additional information
0.065 +/-0.007 micromol/min/ml, hCG-beta by mutant GalNAc-T2-D541A, pH7.4
additional information
0.066 +/-0.008 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D541A, pH7.4
additional information
0.066 +/-0.008 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D541A, pH7.4
additional information
0.066 +/-0.008 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D541A, pH7.4
additional information
0.066 +/-0.008 micromol/min/ml, erythropoitin T by mutant GalNAc-T2-D541A, pH7.4
additional information
0.074 +/-0.005 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.074 +/-0.005 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.074 +/-0.005 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.074 +/-0.005 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.076 +/-0.003 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.076 +/-0.003 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.076 +/-0.003 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.076 +/-0.003 micromol/min/ml, erythropoitin T, pH7.4
additional information
0.094 +/-0.008 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D458H, pH7.4
additional information
0.094 +/-0.008 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D458H, pH7.4
additional information
0.094 +/-0.008 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D458H, pH7.4
additional information
0.094 +/-0.008 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D458H, pH7.4
additional information
0.108 +/-0.002 micromol/min/ml, OSM fragment, pH7.4
additional information
0.108 +/-0.002 micromol/min/ml, OSM fragment, pH7.4
additional information
0.108 +/-0.002 micromol/min/ml, OSM fragment, pH7.4
additional information
0.108 +/-0.002 micromol/min/ml, OSM fragment, pH7.4
additional information
0.121 +/-0.013 micromol/min/ml, MUC1 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.121 +/-0.013 micromol/min/ml, MUC1 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.121 +/-0.013 micromol/min/ml, MUC1 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.121 +/-0.013 micromol/min/ml, MUC1 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.142 +/-0.005 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D541A, pH7.4
additional information
0.142 +/-0.005 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D541A, pH7.4
additional information
0.142 +/-0.005 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D541A, pH7.4
additional information
0.142 +/-0.005 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D541A, pH7.4
additional information
0.151 +/-0.012 micromol/min/ml, MUC1 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.151 +/-0.012 micromol/min/ml, MUC1 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.151 +/-0.012 micromol/min/ml, MUC1 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.151 +/-0.012 micromol/min/ml, MUC1 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.164 +/-0.007 micromol/min/ml, MUC2 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.164 +/-0.007 micromol/min/ml, MUC2 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.164 +/-0.007 micromol/min/ml, MUC2 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.164 +/-0.007 micromol/min/ml, MUC2 by mutant GalNAc-T2-D458H, pH7.4
additional information
0.165 +/-0.013 micromol/min/ml, MUC2 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.165 +/-0.013 micromol/min/ml, MUC2 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.165 +/-0.013 micromol/min/ml, MUC2 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.165 +/-0.013 micromol/min/ml, MUC2 by mutant GalNAc-T2-D541A, pH7.4
additional information
0.185 +/-0.006 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D458H, pH7.4
additional information
0.185 +/-0.006 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D458H, pH7.4
additional information
0.185 +/-0.006 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D458H, pH7.4
additional information
0.185 +/-0.006 micromol/min/ml, IgA hinge by mutant GalNAc-T2-D458H, pH7.4
additional information
128 +/-0.007 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D541A, pH7.4
additional information
128 +/-0.007 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D541A, pH7.4
additional information
128 +/-0.007 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D541A, pH7.4
additional information
128 +/-0.007 micromol/min/ml, MUC1-b' by mutant GalNAc-T2-D541A, pH7.4
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of ppGalNAc-T1, -T2, -T3, -T4, -T6 and -T9 in B-cells and IgA-bearing B cells
-
ascending right part, low enzyme expression, decreased activity compared to normal colon, mono-glycosylates MUC5AC peptide
-
ascending right part, high enzyme expression, 2fold higher activity than in stomach
-
high enzyme expression in tumoral gastric tissue displaying intestinal metaplasia, increased activity compared to normal stomach, di-glycosylates MUC5AC peptide
-
expression analysis of ppGalNAc-T6 in gastric mucosa, intestinal metaplasia, and gastric carcinomas, the isozyme shows a heterogeneous expression and staining pattern
-
stomach fundus, 2fold lower activity than in colon, mono-glycosylates MUC5AC peptide
-
expression of ppGalNAc-T1, -T2, -T3, -T4, -T6 and -T9 in NCI-H929 IgA myeloma cells
ppGalNAc-T13 is abundantly expressed in neuroblastoma cells
immunohistology with a monoclonal antibody shows the expected Golgi-like localization in salivary glands
Northern blot analysis of human tissues
additional information
benign cell line HMT 3522, non-metastatic cell line BT 474, metastatic cell lines ZR75-1, T-47D, MCF-7
ppGalNAc-T3 nearly undetectable in breast cancer cell line HMT-3522
-
brain-specific expression of GalNAc-T9, mRNA is most abundant in cerebellum, lower levels in cerebral cortex, frontal lobe, temporal lobe and putamen
ppGalNAc-T13 is highly and restrictively expressed in brain, fetal brain, adult cerebellum and cerebral cortex, exclusively in neuronal cells
high levels of expression in cerebellum, hippocampus, thalamus, and cerebral cortex. Expression is associated with neurons, but not with glial cells
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
benign cell line HMT 3522, non-metastatic cell line BT 474, metastatic cell lines ZR75-1, T-47D, MCF-7
ppGalNAc-T1 detection in all studied breast cancer cell lines
ppGalNAc-T2 detection in all studied breast cancer cell lines
ppGalNAc-T4 undetectable in breast cancer cell line ZR75-1 cell
ppGalNAc-T6 nearly undetectable in breast cancer cell line HMT-3522
-
human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T1
-
human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T2
-
human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T3
-
human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T1
-
human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T2
-
human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T3
-
human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T4
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
very weak signal, nearly undetectable
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
gastric cancer cell line, cDNA encoding the transferase is cloned and sequenced from a cDNA library of a human cancer cell line
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
-
expression analysis of ppGalNAc-T6 in gastric mucosa, intestinal metaplasia, and gastric carcinomas
additional information
-
quantitative and qualitative differences in different organs
additional information
-
existence of more than one form of GalNAc-Ts which are expressed differentially in the gastrointestinal tract
additional information
tissue distribution of several ppGalNAc-transferases
additional information
-
ppGalNAc-T1 is ubiquitously expressed, ppGalNAc-T13: not in glioblastoma cells and primary cultured astrocytes
additional information
ppGalNAc-T1 is ubiquitously expressed, ppGalNAc-T13: not in glioblastoma cells and primary cultured astrocytes
additional information
-
no activity of GalNAc-T6 in GP202 cells and GP220 cells
additional information
-
no activity of GalNAc-T6 in MKN45 cells, GP202 cells, GP220 cells, and K562
additional information
pp-GalNAc-T15 transcript is ubiquitously expressed in human tissues, very low activity in bone marrow, leukocyte, heart, liver, testis, enzyme form pp-GalNAc-T15
additional information
pp-GalNAc-T15 transcript is ubiquitously expressed in human tissues, very low activity in bone marrow, leukocyte, heart, liver, testis, enzyme form pp-GalNAc-T15
additional information
-
pp-GalNAc-T15 transcript is ubiquitously expressed in human tissues, very low activity in bone marrow, leukocyte, heart, liver, testis, enzyme form pp-GalNAc-T15
additional information
Northern analysis of human organs revealed a wide expression pattern
additional information
Northern analysis of human organs revealed a wide expression pattern
additional information
Northern analysis of human organs revealed a wide expression pattern
additional information
-
Northern analysis of human organs revealed a wide expression pattern
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
immunocytochemical detection using an isozyme-specific mouse monoclonal antibody
additional information
immunocytochemical detection using an isozyme-specific mouse monoclonal antibody
CHO ldlD-MUC1 cells in presence of GalNAc
CHO ldlD-MUC1 cells in presence of GalNAc: same pattern of biotinylated GalNAc-T2 like Tn (GalNAc-alpha-Ser/Thr)
CHO ldlD-MUC1 cells in presence of GalNAc: same pattern of biotinylated GalNAc-T4 and -T4 lectin like Tn (GalNAc-alpha-Ser/Thr)
human salivary glands: same pattern of biotinylated GalNAc-T2 at Golgi-like supranuclear locations like Tn (GalNAc-alpha-Ser/Thr)
human salivary glands: same pattern of biotinylated GalNAc-T4 lectin at Golgi-like supranuclear locations like Tn (GalNAc-alpha-Ser/Thr)
GalNAc-T7: type II transmembrane protein with a hydrophobic signal anchor sequence in residues 10-24
-
GalNAc-T9: type II membrane protein with a 20-amino acid transmembrane domain, a 7-amino acid cytoplasmic domain and a 91-amino acid stem region
ppGaNTase-T13: type II membrane protein with a 20-amino acid transmembrane segment and an 8-amino acid N-terminal cytoplasmic domain
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
additional information
distinct localisation of ppGalNAc-Ts in different breast cancer cell lines
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
GalNAc-type protein O-glycosylation is important in modulating protein processing, O-linked glycans have important biological functions
physiological function
malfunction
-
aberrant mucin O-glycosylation is often observed in cancer and is characterized by the expression of immature simple mucin-type carbohydrate antigens. Altered expression of ppGalNAc-Ts can be one of the mechanisms that explain the changes in mucin O-glycosylation during malignant transformation
malfunction
mutation of the enzyme might be involved in development of cancer
malfunction
-
Overexpression of polypeptide N-acetylgalactosaminyltransferase 6 induces epithelial-to-mesenchymal transition-like morphologic alterations
malfunction
-
knockdown of the isoform GALNT3 expression in epithelial ovarian cancer cells leads to sharp decrease of cell proliferation and induced S-phase cell cycle arrest. Additionally, GALNT3 suppression significantly inhibits epithelial ovarian cancer cell migration and invasion. GALNT3 knockdown is also accompanied with increase of the cell adhesion molecules beta-catenin and E-cadherin
physiological function
-
ppGalNAc-T6 is one of the enzymes responsible for the initial step in mucin O-glycosylation
physiological function
the GALNT enzyme plays a role in initiating mucin type O-linked protein glycosylation
physiological function
-
site-specific O-glycosylation inhibits proprotein activation of the lipase inhibitor ANGPTL3 in HepG2 cells
physiological function
-
the lectin domain strictly recognizes GalNAc on the substrate and this specificity controls the glycosylation pathway
physiological function
-
isoform GALNT14 contributes to ovarian carcinogenesis through aberrant glycosylation of MUC13, but not through the interleukin-8 pathway
physiological function
-
the enzyme is involved in disorders of lipid metabolism
physiological function
GalNAc-T18 silencing in cells decreases O-glycosylation levels and activates ER stress leading to apoptosis. After treatment with chaperone 4-phenylbutyric acid or forced expression of GalNAc-T18 in the GalNAc-T18 knockdown cell, these defects can be significantly alleviated. GalNAc-T18 exerts its functions in O-glycosylation and ER stress via a non-catalytic mechanism. Both wild-type GalNT18 and mutant H253D show no catalytic activity in vitro, but both of them can rescue the O-glycosylation defect of GalNAc-T18 knockdown cells
physiological function
isoform GalNAc-T1 is largely required for the Ebola virus surface glycoprotein-mediated adhesion defects. Despite its profound effect on surface glycoprotein function, the absence of GalNAc-T1 only modestly reduces the O-glycan mass of surface glycoprotein. A small segment of the mucin-like domain of the surface glycoprotein is critical for function and mutation of five glycan acceptor sites within this segment are sufficient to abrogate surface glycoprotein function
physiological function
isoform GalNAc-T11-specific glycosites are glycosylated in a dose-dependent manner and induction of GalNAc-T11 produces discrete glycosylation effects without affecting the major part of the O-glycoproteome. Responder proteins are the LA-2 module in VLDLR (70KTCAESDFVCNNGQCVPSR88), a glycosite just C-terminal to the single LA module in SPINT1 (328HPVCSGTCQPTQFR341), a class A repeat in LRP1 (873CDGDNDCLDNSDEAPALCHQHTCPSDR899), BCR-associated protein 29/BCAP29, cathepsin D/CTSD, neuferricin/CYB5D2, HLA-A, GRP-78/HSPA5/BiP, podocalyxin/PODXL, xyloside xylosyltransferase 1/XXYLT1, and golgin 1/GLG1
physiological function
isoform GalNAc-T2 is the specific regulator of O-glycosylation of Ser6, Ser25 and Ser29 in the N-terminal ectodomain of the receptor. Single-nucleotide polymorphism F27C of the receptor alters O-glycosylation of the receptor in efficiency as well as in glycosite usage. The absence of O-glycans results in decreased receptor levels at the plasma membrane due to enhanced turnover. Mutation of the identified O-glycosylation sites leads to a decrease in the number of ligand binding competent receptors and impaired agonist-mediated inhibition of cyclic AMP accumulation in HEK-293 cells
physiological function
isoform GalNAc-T2-specific glycosites are glycosylated in a dose-dependent manner and induction of GalNAc-T2 produces discrete glycosylation effects without affecting the major part of the O-glycoproteome. Responder proteins are GRP-78/HSPA5/BiP (634LYGSAGPPPTGEEDTAEKDEL654), PAPS transporter 1/SLC35B2 (137SYGATATSPGER148), 4Gal-T3/B4GALT3 (219SFPDQFSTGEPPALDEVPEVR239) (ambiguous glycosites italicized), calnexin/CANX (62APVPTGEVYFADSFDR77), GP73/GOLM1 (233SQTPAPSSEVVLDSK247 and 233SQTPAPSSE241), LRP11 (299AAYSTGGCLHTCSR312), TGN46/TGOLN2 (346MSGSASSENR355), and carboxypeptidase D/CPD (219SFPDQFSTGEPPALDEVPEVR239)
physiological function
polypeptide GalNAc-transferase 2 specifically O-glycosylates beta1-adrenergic receptor at five residues in the extracellular N-terminus, including the Ser49 residue at the location of the common S49G single-nucleotide polymorphism. GalNAc-T2 coregulates the metalloproteinase-mediated limited proteolysis of beta1-adrenergic receptor. Impaired O-glycosylation and enhanced proteolysis lead to attenuated receptor signaling
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GALT3_HUMAN
633
1
72610
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
single band, SDS-PAGE. Polymerase chain reaction cloning and sequencing of the human version of the bovine transferase are presented, and 98% similarity at the amino acid level is found
59210
molecular mass of the deduced amino acid sequence of the soluble transferase is 59205 Da, which is slightly higher than the experimentally determined molecular weight but within the limits of accuracy of the SDS-PAGE and gel filtration systems used
61000
64700
cDNA sequence has a 571-amino acid coding region indicating a protein of 64.7 kDa with a type II domain structure
87000
61000
endogenous GalNAc-T14 in HEK293T cells detected by anti-GalNAc-T14 antibody
61000
Flag-tag fusion protein expressed in HEK293T cells detected by anti-Flag and anti-GalNAc-T14 antibody
87000
bacterially expressed GST-fusion protein (GST: 26 kDa) detected by anti-GST and anti-GalNAc-T14 antibody
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme activity is reduced up to 95% by in vitro acetylation of residue K103, S109, K111, K363, S373, K521 and S529
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dynamics of loop B reduced upon UDP-GalNAc (donor) binding but not further reduced by subsequent peptide (acceptor) binding
flexibility of terminal residues of EA2 peptide in EA2-enzyme complex is reduced upon presence of a GalNAc moiety
hanging drop vapor diffusion at room temperature. X-ray crystal structures of the enzyme bound to the product UDP at 2.75 A resolution and to UDP and an acceptor peptide substrate EA2 (PTTDSTTPAPTTK) at 1.64 A resolution
-
in presence of UDP or UDP and peptide no water molecule-dependent, large conformational changes
PDB: 2FFU incl. substrates versus PDB: 2FFU lacking substrates: flexibility of catalytic and lectin domain independent of each others presence or distance
PDB: 2FFV versus PDB: 2FFU: large conformational changes (13 to 24 Å) in catalytic domain upon peptide binding and processing, loop A (AA89-98), loop B (AA361-377)
PDB: 2FFV versus PDB: 2FFU: small conformational changes (4 to 5 Å) of protein backbone upon peptide binding and processing, loop C (AA127-134), loop D (AA287-297), loop E (AA330-333)
single-displacement transfer mechanism revealed by simulations on crystal structure PDB: 2FFU
structures of GalNAc-T7, and of its complex with the donor substrate UDP-GalNAc. The N-terminal catalytic domain and C-terminal lectin domain are connected by a flexible linker, forming a narrow cleft for the acceptor substrate. Only the alpha subdomain of the lectin domain binds to the glycosyl group. Compared to the apo structure, the loop covering the catalytic center of the complex show significant conformational changes
water molecule-dependent rotation of W331 side chain (WGGEN motif within loop E) that triggers loop B opening in the absence of substrate UDP-GalNAc and facilitates donor access into the active site as well as product release
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D261N
naturally occuring mutation, the mutant activity is slightly reduced compared to the wild-type enzyme
D303N
naturally occuring mutation, the mutant activity is reduced by 60% compared to the wild-type enzyme
E119V
naturally occuring mutation, the mutant activity is slightly increased compared to the wild-type enzyme
E334Q
the mutant shows strongly reduced activity compared to the wild type enzyme
G272R
naturally occuring mutation, the mutant activity is slightly reduced compared to the wild-type enzyme
G3E
naturally occuring mutation, the mutant activity is slightly reduced compared to the wild-type enzyme
G46R
naturally occuring mutation, the mutant activity is unaltered compared to the wild-type enzyme
GalNAc-T2 lectin domain
amino acids 405 to 578 of GalNAc-T2, lower expression level than full-length enzyme
GalNAc-T2-D224H
mutation in DXH nucleotide-binding motif, inactive mutant
GalNAc-T2-D458H
mutation in CLD motif of alpha repeat, impaired lectin-mediated MUC1 and GalNAc-MUC1 binding, no impaired specific activity, incorporates 1-2 fewer GalNAc residues per substrate molecule in endpoint reactions, no utilization of partially GalNAc-glycosylated peptides, higher KM for IgA hinge-4GalNAc
GalNAc-T2-D541A
mutation in CLD motif of gamma repeat
GalNAc-T4 lectin domain
amino acids 432 to 571 of GalNAc-T4, lower expression level than full-length enzyme
GalNAc-T4 lectin domain-D459H
mutation in CLD motif of alpha repeat
GalNAc-T4-D459H
mutation in CLD motif of alpha repeat, impaired lectin-mediated MUC1 and GalNAc-MUC1 binding
hT10CD
-
GalNAc-T10 catalytic domain, hT10 lacking lectin domain (AA446-603) and transmembrane domain (AA1-70), no altered preference in glycosylation site selection, loss of initial burst phase during glycosylation of MUC5AC-13 at Thr-9, gain of initial burst phase during glycosylation of MUC5AC-3 at Thr-9, GalNAc-transfer accompanied by high rate of UDP-GalNAc hydrolysis, lectin domain not required for catalysis, no glycosylation of MUC5AC-9
hT10CD-hT2LD
-
GalNAc-T10 catalytic domain-GalNAc-T2 lectin domain, hT10 lacking lectin domain (AA446-603) and transmembrane domain (AA1-70) fused to hT2 lectin domain, no glycosylation of MUC5AC-9
hT2CD
-
GalNAc-T2 catalytic domain, hT2 lacking lectin domain (AA441-571) and transmembrane domain (AA1-74), reduced affinity for substrate MUC5AC-13 but not for MUC5AC-3, shift of preferred MUC5AC-3 glycosylation site from Thr-9 to Thr-13
hT2CD-hT10LD
-
GalNAc-T2 catalytic domain-GalNAc-T10 lectin domain, hT2 lacking lectin domain (AA441-571) and transmembrane domain (AA1-74) fused to hT10 lectin domain, partially restored glycosylation to Thr-3 on MUC5AC-13 but not to Thr-13 on MUC5AC-3 or Ser-5 on MUC5AC-3,13
I253A/L310A
UDP-GalNAc is a poor substrate, some UDP-GalNAc analogs with longer or branched N-acyl chains are better substrates for mutant I253A/L310A than for wild-type
K521Q
-
the mutation enhances the carbohydrate specificity of lectin domain for alpha-GalNAc and results in reduced enzyme activity compared to the wild type enzyme
N335A
the mutant shows strongly reduced activity compared to the wild type enzyme
N335D
the mutant shows strongly reduced activity compared to the wild type enzyme
N335H
the mutant shows strongly reduced activity compared to the wild type enzyme
N335S
the mutant shows strongly reduced activity compared to the wild type enzyme
R297W
naturally occuring mutation, the mutant activity is reduced by about 95% compared to the wild-type enzyme
R362K
the mutant shows strongly reduced activity compared to the wild type enzyme
R373H
naturally occuring mutation, the mutant activity is reduced by about 97% compared to the wild-type enzyme
R382H
naturally occuring mutation, the mutant activity is almost completely inactive
R552K
naturally occuring mutation, the mutant activity is unaltered compared to the wild-type enzyme
T491M
naturally occuring mutation, the mutant activity is reduced by about 98% compared to the wild-type enzyme
additional information
additional information
linkage analysis of GalNAc-T4 with the base pair G1516A substitution
additional information
linkage analysis of GalNAc-T4 with the base pair G1516A substitution
additional information
linkage analysis of GalNAc-T4 with the base pair G1516A substitution
additional information
-
linkage analysis of GalNAc-T4 with the base pair G1516A substitution
additional information
identification of somatic and germ-line mutations in GALNT12 in individuals with colon cancer, each of the 8 GALNT12 mutations identified inactivates the normal function of the GALNT enzyme in initiating mucin type O-linked protein glycosylation, overview
additional information
-
identification of somatic and germ-line mutations in GALNT12 in individuals with colon cancer, each of the 8 GALNT12 mutations identified inactivates the normal function of the GALNT enzyme in initiating mucin type O-linked protein glycosylation, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
24 h, GalNAc-T1 and -T3: 40% loss of activity, GalNAc-T2: 60% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
23% loss of specific activity after 12h shaking at 37°C
25% loss of specific activity after 12 h shaking at 37°C
31% loss of specific activity after 12h shaking at 37°C
mutant GalNAc-T2-D458H: 15% loss of specific activity after 12h shaking at 37°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anti-FLAG m2 affinity chromatography
GST fusion protein purified by affinity chromatography, elution with 10 mM glutathione, pH8
placenta enzyme, Muc2 peptide affinity chromatography separates two distinct transferase activities with overlapping specificity concerning Muc2 substrate, but which are distinguishable with respect to HIV-V3 substrate
-
purification of His-tagged truncated lectin domain by IMAC, 250 mM imidazole
purification of secreted recombinant proteins from cell culture supernatant by Amberlite IRA-95 chromatography followed by SP Sepharose Fast Flow ion-exchange chromatography and concentrated by centrifugation through 10000 Da cut-off filter followed by elution from a PC3.2/3 column
purified to apparent homogeneity using a synthetic acceptor peptide as affinity ligand
recombinant ppGalNAc-T1, -T2, -T3, -T4, -T6 and T9, expressed in insect cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of ppGalNAc-T1, -T2, -T3, -T4, -T6 and T9 and expression as secreted proteins fused with a FLAG peptide in insect cells
-
expressed in Sf9 cells or in a stably transfected Chinese hamster ovary cell line exhibited a unique acceptor substrate specificity
expressed in Sf9 cells, expressed in a stably transfected Chinese hamster ovary cell line exhibited a unique acceptor substrate specificity, expressed in High Five cells
expression of GalNAc-T1, -T2 and -T3 as soluble proteins in insect Sf9 cells
-
FLAG fusion protein (amino acid residue 42-607 (catalytic region and lectin domain)) expressed in HEK293T cells
full-length GalNAc-T14 in pGEX-4T-1, expression in Escherichia coli BL21(DE3)
GalNAc-T7 is cloned and expressed in insect Sf9 cells, open reading frame of 1974 bp, GALNT7 gene encoding GalNAc-T7 is localized on chromosome 4q31.1
GalNAc-T9 is cloned and characterized encoding a 603 amino acid protein, nucleotide and amino acid sequence
-
GALNT12, DNA and amino acid sequence determination and analysis, genotyping, recombinant expression of tagged wild-type and mutant enzymes
in pAcGP67-His vector for amplification as bacculovirus in Sf9 cells and subsequent infection of High Five cells
in pKN55-N6His-TEV for expression in Pichia pastoris strain SMD1168 and with TEV-cleavable hexa-His-tag
-
PCR cloning of human version of GalNAc-T1, based on the reported sequence of bovine GalNAc-T1. Polymerase chain reaction cloning and sequencing of the human version of the bovine transferase are presented, and 98% similarity at the amino acid level is found
PCR construct is expressed in insect cells using a baculovirus vector. Expression of GalNAc-T2 in Sf9 cells
ppGalNAc-T13, -T1 and -T9 are cloned, and expressed in Sf21 or High FiveTM insect cells in a soluble form, ppGalNAc-T13: gene is localized to chromosome 2, nucleotide sequence encodes a 556-amino acid protein, ppGalNAc-T1 is localized to chromosome 18
ppGalNAc-T14 and -T2 are cloned and expressed in Sf21 cells in a secreted form, 2 alternatively spliced isoforms of the ppGalNAc-T14 transcript are sequenced, major splicing form: 552-amino acid protein, ppGalNAc-T14 gene is mapped to chromosome 2p23.2
-
recombinant human pt-GalNAc-T, which is expressed in insect cells, does not glycosylate several peptides derived from mammalian mucins
soluble His-tagged protein (cytosolic tail and transmembrane domain removed) expressed in Sf9 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform GalNAc-T3 is highly expressed in papillary carcinomas that have invaded beyond the thyroid capsule
extracellular signal-regulated kinase 1/2 inhibitor modulates the expression levels of isoform GALNT14
-
isoform GALNT3 is strongly overexpressed in high-grade serous epithelial ovarian tumors as compared to normal ovarian tissue
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
isoform GalNAc-T3 expression is an indicator of tumor differentiation in thyroid carcinoma
analysis
drug development
medicine
molecular biology
analysis
development of a bump-hole chemical reporter system for studying GalNAc-T activity in vitro. GalNAc-T2 ire rationally engineered to contain an enlarged active site (hole) and probed with a collection of 20 (bumped) uridine diphosphate N-acetylgalactosamine analogs to identify enzyme-substrate pairs that retain peptide specificities but are otherwise completely orthogonal to native enzyme-substrate pairs. The approach is applicable to multiple GalNAc-T isoenzymes, including GalNAc-T1 and -T2 that prefer nonglycosylated peptide substrates and GalNAcT-10 that prefers a preglycosylated peptide substrate
analysis
development of isogenic cell-model systems withTet-On inducible expression of GalNAc-T genes GALNT2 and GALNT11 in a knockout background in HEK-293 cells to identify O-glycopeptides differentially affected by induction of GalNAc-T2 or -T11
drug development
further studies of the substrate specificity of these and potentially additional enzymes are required, but it may be anticipated that this understanding will be significant for insight into O-glycosylation processing and of practical use, for example, for designing appropriate mammalian expression systems for recombinant glycoproteins in drug use
drug development
further studies of the substrate specificity of these and potentially additional enzymes are required, but it may be anticipated that this understanding will be significant for our insight into O-glycosylation processing and of practical use, for example, for designing appropriate mammalian expression systems for recombinant glycoproteins in drug use
medicine
-
cancer cells compared to normal cells exhibit altered glycosyltransferase activities, enzyme is a new tool for the investigation of motif peptide O-glycosylation alterations in pathological situations
medicine
-
isoform GALNT3 expression significantly correlates with shorter progression-free survival intervals in epithelial ovarian cancer patients with advanced disease
medicine
isoform GalNAc-T1 is largely required for the Ebola virus surface glycoprotein-mediated adhesion defects. Despite its profound effect on surface glycoprotein function, the absence of GalNAc-T1 only modestly reduces the O-glycan mass of surface glycoprotein. A small segment of the mucin-like domain of the surface glycoprotein is critical for function and mutation of five glycan acceptor sites within this segment are sufficient to abrogate surface glycoprotein function
medicine
isoform GalNAc-T4 shows a stage-dependent expression at the different stages of colorectal cancer in 62 pair-matched tumor/normal tissues. GalNAc-T4 expression is significantly induced at stage I and II but not at stage III and IV. Overexpression of GalNAc-T4 in colorectal cancer cells enhances colony formation and sphere formation. Knockdown of GalNAc-T4 in colorectal cancer cells increases the cell migration and invasion, and leads to an epithelial-mesenchymal transition-like transition. Loss of GalNAc-T4 contributes to the dedifferentiation of colorectal cancer cells and high expression of GalNAc-T4 correlates to a good prognosis of patients
molecular biology
enzyme-linked lectin assay (ELLA) as carbohydrate-binding assay
molecular biology
polyclonal rabbit anti-GalNAc-T14 IgG (1: 1000 in Western blot, titer: appr. 1: 16000) for study of expression and distribution of human GalNAc-T14
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Soerensen, T.; White, T.; Wandall, H.H.; Kristensen, A.K.; Roepstorff, P.; Clausen, H.
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Identification and separation of two distinct transferase activities
J. Biol. Chem.
270
24166-24173
1995
Homo sapiens, Ovis sp., Rattus norvegicus, Sus scrofa
Wandall, H.H.; Hassan, H.; Mirgorodskaya, E.; Kristensen, A.K.; Roepstorff, P.; Bennett, E.P.; Nielsen, P.A.; Hollingsworth, M.A.; Burchell, J.; Taylor-Papadimitriou, J.; Clausen, H.
Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3
J. Biol. Chem.
272
23503-23514
1997
Homo sapiens
Bennett, E.P.; Hassan, H.; Hollingsworth, M.A.; Clausen, H.
A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates
FEBS Lett.
460
226-230
1999
Homo sapiens (Q86SF2), Homo sapiens
Toba, S.; Tenno, M.; Konishi, M.; Mikami, T.; Itoh, N.; Kurosaka, A.
Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9)
Biochim. Biophys. Acta
1493
264-268
2000
Homo sapiens
Wang, H.; Tachibana, K.; Zhang, Y.; Iwasaki, H.; Kameyama, A.; Cheng, L.; Guo, J.; Hiruma, T.; Togayachi, A.; Kudo, T.; Kikuchi, N.; Narimatsu, H.
Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14
Biochem. Biophys. Res. Commun.
300
738-744
2003
Homo sapiens
Zhang, Y.; Iwasaki, H.; Wang, H.; Kudo, T.; Kalka, T.B.; Hennet, T.; Kubota, T.; Cheng, L.; Inaba, N.; Gotoh, M.; Togayachi, A.; Guo, J.; Hisatomi, H.; Nakajima, K.; Nishihara, S.; Nakamura, M.; Marth, J.D.; Narimatsu, H.
Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen
J. Biol. Chem.
278
573-584
2003
Homo sapiens, Homo sapiens (Q8IUC8), Mus musculus
Hanisch, F.G.; Reis, C.A.; Clausen, H.; Paulsen, H.
Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides
Glycobiology
11
731-740
2001
Homo sapiens
Iwasaki, H.; Zhang, Y.; Tachibana, K.; Gotoh, M.; Kikuchi, N.; Kwon, Y.D.; Togayachi, A.; Kudo, T.; Kubota, T.; Narimatsu, H.
Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2
J. Biol. Chem.
278
5613-5621
2003
Homo sapiens
Hennebicq, S.; Tetaert, D.; Soudan, B.; Briand, G.; Richet, C.; Demeyer, D.; Gagnon, J.; Petillot, Y.; Degand, P.
Polypeptide:N-acetylgalactosaminyltransferase activities towards the mucin MUC5AC peptide motif using microsomal preparations of normal and tumoral digestive mucosa
Biochimie
80
69-73
1998
Homo sapiens
Takeuchi, H.; Kato, K.; Hassan, H.; Clausen, H.; Irimura, T.
O-GalNAc incorporation into a cluster acceptor site of three consecutive threonines. Distinct specificity of GalNAc-transferase isoforms
Eur. J. Biochem.
269
6173-6183
2002
Homo sapiens
Katao, K.; Takeuchi, H.; Miyahara, N.; Kanoh, A.; Hassan, H.; Clausen, H.; Irimura, T.
Distinct orders of GalNAc incorporation into a peptide with consecutive threonines
Biochem. Biophys. Res. Commun.
287
110-115
2001
Homo sapiens
Iida, S.I.; Takeuchi, H.; Kato, K.; Yamamoto, K.; Irimura, T.
Order and maximum incorporation of N-acetyl-D-galactosamine into threonine residues of MUC2 core peptide with microsome fraction of human-colon-carcinoma LS174T cells
Biochem. J.
347
535-542
2000
Homo sapiens
Nishimaori, I.; Fontenot, J.D.; Hollingsworth, M.A.
N-Acetylgalactosamine glycosylation of MUC1 tandem repeat peptides by pancreatic tumor cell extracts
Cancer Res.
54
3738-3744
1994
Homo sapiens
Marcos, N.T.; Cruz, A.; Silva, F.; Almeida, R.; David, L.; Mandel, U.; Clausen, H.; von Mensdorff-Pouilly, S.; Reis, C.A.
Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines
J. Histochem. Cytochem.
51
761-771
2003
Homo sapiens
Nakamura, N.; Toba, S.; Hirai, M.; Morishita, S.; Mikami, T.; Konishi, M.; Itoh, N.; Kurosaka, A.
Cloning and expression of a brain-specific putative UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase gene
Biol. Pharm. Bull.
28
429-433
2005
Rattus norvegicus, Homo sapiens (Q9HCQ5), Homo sapiens
Guo, J.M.; Zhang, Y.; Cheng, L.; Iwasaki, H.; Wang, H.; Kubota, T.; Tachibana, K.; Narimatsu, H.
Molecular cloning; characterization of a novel member of the UDP-GalNAc polypeptide N-acetylgalactosaminyltransferase family,ppGalNAc-T12
FEBS Lett.
26297
1-8
2002
Homo sapiens (Q8IXK2)
-
Cheng, L.; Tachibana, K.; Iwasaki, H.; Kameyama, A.; Zhang, Y.; Kubota, T.; Hiruma, T.; Kudo, T.; Guo, J.M.; Narimatsu, H.
Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15
FEBS Lett.
566
17-24
2004
Homo sapiens (Q10471), Homo sapiens (Q7Z4T8), Homo sapiens
White, T.; Bennett, E.P.; Takio, K.; Sorensen, T.; Bonding, N.; Clausen, H.
Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
J. Biol. Chem.
270
24156-24165
1995
Homo sapiens (Q10471), Homo sapiens (Q10472), Homo sapiens
Bennett, E.P.; Hassan, H.; Clausen, H.
cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosaminyltransferase
J. Biol. Chem.
271
17006-17012
1996
Homo sapiens (Q14435), Homo sapiens
Bennett, R.P.; Hassan, H.; Mandel, U.; Mirgorodskaya, E.; et al.
Cloning of human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat
J. Biol. Chem.
273
30472-30481
1998
Homo sapiens (Q10471), Homo sapiens (Q10472), Homo sapiens (Q8N4A0), Homo sapiens
Bennett, E.P.; Hassan, H.; Mandel, U.; Hollingsworth, M.A.; Akisawa, N.; Ikematsu, Y.; Merkx, G.; van Kessel, A.G.; Olofsson, S.; Clausen, H.
Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6
J. Biol. Chem.
274
25362-25370
1999
Homo sapiens (Q8NCL4), Homo sapiens
Sschwientek, T.; Bennett, E.P.; Flores, C.; et al.
Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans and mammals
J. Biol. Chem.
277
22623-22638
2002
Homo sapiens (Q8NCW6), Homo sapiens
Fritz, T.A.; Raman, J.; Tabak, L.A.
Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2
J. Biol. Chem.
281
8613-8619
2006
Homo sapiens
Brooks, S.A.; Carter, T.M.; Bennett, E.P.; Clausen, H.; Mandel, U.
Immunolocalisation of members of the polypeptide N-acetylgalactosaminyl transferase (ppGalNAc-T) family is consistent with biologically relevant altered cell surface glycosylation in breast cancer
Acta Histochem.
109
273-284
2007
Homo sapiens (Q10471), Homo sapiens (Q10472), Homo sapiens (Q14435), Homo sapiens (Q8N4A0), Homo sapiens (Q8NCL4)
Wandall, H.H.; Irazoqui, F.; Tarp, M.A.; Bennett, E.P.; Mandel, U.; Takeuchi, H.; Kato, K.; Irimura, T.; Suryanarayanan, G.; Hollingsworth, M.A.; Clausen, H.
The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation
Glycobiology
17
374-387
2007
Homo sapiens (Q10471), Homo sapiens (Q10472), Homo sapiens (Q8N4A0), Homo sapiens (Q8NCW6)
Gerken, T.A.; Hagen, K.G.; Jamison, O.
Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase orthologue pairs
Glycobiology
18
861-870
2008
Bos taurus (Q07537), Homo sapiens (Q10471), Drosophila melanogaster (Q6WV17), Drosophila melanogaster (Q6WV19)
Raman, J.; Fritz, T.A.; Gerken, T.A.; Jamison, O.; Live, D.; Liu, M.; Tabak, L.A.
The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase function in concert to direct glycosylation site selection
J. Biol. Chem.
283
22942-22951
2008
Homo sapiens
Milac, A.L.; Buchete, N.V.; Fritz, T.A.; Hummer, G.; Tabak, L.A.
Substrate-induced conformational changes and dynamics of UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase-2
J. Mol. Biol.
373
439-451
2007
Homo sapiens (Q10471)
Wu, C.; Wang, Y.; Zou, M.; Shan, Y.; Yao, G.; Wei, P.; Chen, G.; Wang, J.; Xu, D.
Prokaryotic expression, purification, and production of polyclonal antibody against human polypeptide N-acetylgalactosaminyltransferase 14
Protein Expr. Purif.
56
1-7
2007
Homo sapiens (Q96FL9), Homo sapiens
Brockhausen, I.; Dowler, T.; Paulsen, H.
Site directed processing: role of amino acid sequences and glycosylation of acceptor glycopeptides in the assembly of extended mucin type O-glycan core 2
Biochim. Biophys. Acta
1790
1244-1257
2009
Bos taurus, Homo sapiens (Q10472)
Perrine, C.L.; Ganguli, A.; Wu, P.; Bertozzi, C.R.; Fritz, T.A.; Raman, J.; Tabak, L.A.; Gerken, T.A.
Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2
J. Biol. Chem.
284
20387-20397
2009
Bos taurus, Homo sapiens
Gomes, J.; Marcos, N.T.; Berois, N.; Osinaga, E.; Magalhaes, A.; Pinto-de-Sousa, J.; Almeida, R.; Gaertner, F.; Reis, C.A.
Expression of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6 in gastric mucosa, intestinal metaplasia, and gastric carcinoma
J. Histochem. Cytochem.
57
79-86
2009
Homo sapiens
Guda, K.; Moinova, H.; He, J.; Jamison, O.; Ravi, L.; Natale, L.; Lutterbaugh, J.; Lawrence, E.; Lewis, S.; Willson, J.K.; Lowe, J.B.; Wiesner, G.L.; Parmigiani, G.; Barnholtz-Sloan, J.; Dawson, D.W.; Velculescu, V.E.; Kinzler, K.W.; Papadopoulos, N.; Vogelstein, B.; Willis, J.; Gerken, T.A.; Markowitz,
Inactivating germ-line and somatic mutations in polypeptide N-acetylgalactosaminyltransferase 12 in human colon cancers
Proc. Natl. Acad. Sci. USA
106
12921-12925
2009
Homo sapiens (Q8IXK2), Homo sapiens
Zlocowski, N.; Sendra, V.G.; Lorenz, V.; Villarreal, M.A.; Jorge, A.; Nunez, Y.; Bennett, E.P.; Clausen, H.; Nores, G.A.; Irazoqui, F.J.
Catalytic and glycan-binding abilities of ppGalNAc-T2 are regulated by acetylation
Biochem. Biophys. Res. Commun.
410
140-145
2011
Homo sapiens
Schjoldager, K.T.; Clausen, H.
Site-specific protein O-glycosylation modulates proprotein processing - Deciphering specific functions of the large polypeptide GalNAc-transferase gene family
Biochim. Biophys. Acta
1820
2079-2094
2012
Homo sapiens
Yoshimura, Y.; Nudelman, A.S.; Levery, S.B.; Wandall, H.H.; Bennett, E.P.; Hindsgaul, O.; Clausen, H.; Nishimura, S.
Elucidation of the sugar recognition ability of the lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 by using unnatural glycopeptide substrates
Glycobiology
22
429-438
2012
Homo sapiens
Li, X.; Wang, J.; Li, W.; Xu, Y.; Shao, D.; Xie, Y.; Xie, W.; Kubota, T.; Narimatsu, H.; Zhang, Y.
Characterization of ppGalNAc-T18, a member of the vertebrate-specific Y subfamily of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases
Glycobiology
22
602-615
2012
Homo sapiens (Q58A54)
Raman, J.; Guan, Y.; Perrine, C.L.; Gerken, T.A.; Tabak, L.A.
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree
Glycobiology
22
768-777
2012
Homo sapiens
Hua, D.; Shen, L.; Xu, L.; Jiang, Z.; Zhou, Y.; Yue, A.; Zou, S.; Cheng, Z.; Wu, S.
Polypeptide N-acetylgalactosaminyltransferase 2 regulates cellular metastasis-associated behavior in gastric cancer
Int. J. Mol. Med.
30
1267-1274
2012
Homo sapiens
Park, J.H.; Katagiri, T.; Chung, S.; Kijima, K.; Nakamura, Y.
Polypeptide N-acetylgalactosaminyltransferase 6 disrupts mammary acinar morphogenesis through O-glycosylation of fibronectin
Neoplasia
13
320-326
2011
Homo sapiens
Schjoldager, K.; Vakhrushev, S.; Kong, Y.; Steentoft, C.; Nudelman, A.; Pedersen, N.; Wandall, H.; Mandel, U.; Bennett, E.; Levery, S.; Clausen, H.
Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells
Proc. Natl. Acad. Sci. USA
109
9893-9898
2012
Homo sapiens
Lira-Navarrete, E.; Iglesias-Fernandez, J.; Zandberg, W.F.; Companon, I.; Kong, Y.; Corzana, F.; Pinto, B.M.; Clausen, H.; Peregrina, J.M.; Vocadlo, D.J.; Rovira, C.; Hurtado-Guerrero, R.
Substrate-guided front-face reaction revealed by combined structural snapshots and metadynamics for the polypeptide N-acetylgalactosaminyltransferase 2
Angew. Chem. Int. Ed. Engl.
53
8206-8210
2014
Homo sapiens
Irazoqui, F.; Zlocowski, N.; Lorenz, V.; Bennett, E.; Clausen, H.; Nores, G.
An acetylation site in lectin domain modulates the biological activity of polypeptide GalNAc-transferase-2
Biol. Chem.
394
69-77
2013
Homo sapiens
Kong, Y.; Joshi, H.J.; Schjoldager, K.T.; Madsen, T.D.; Gerken, T.A.; Vester-Christensen, M.B.; Wandall, H.H.; Bennett, E.P.; Levery, S.B.; Vakhrushev, S.Y.; Clausen, H.
Probing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysis
Glycobiology
25
55-65
2015
Homo sapiens
Gerken, T.A.; Revoredo, L.; Thome, J.J.; Tabak, L.A.; Vester-Christensen, M.B.; Clausen, H.; Gahlay, G.K.; Jarvis, D.L.; Johnson, R.W.; Moniz, H.A.; Moremen, K.
The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation
J. Biol. Chem.
288
19900-19914
2013
Bos taurus, Homo sapiens
Song, L.; Bachert, C.; Schjoldager, K.T.; Clausen, H.; Linstedt, A.D.
Development of isoform-specific sensors of polypeptide GalNAc-transferase activity
J. Biol. Chem.
289
30556-30566
2014
Homo sapiens
Wang, R.; Yu, C.; Zhao, D.; Wu, M.; Yang, Z.
The mucin-type glycosylating enzyme polypeptide N-acetylgalactosaminyltransferase 14 promotes the migration of ovarian cancer by modifying mucin 13
Oncol. Rep.
30
667-676
2013
Homo sapiens
Wang, Z.Q.; Bachvarova, M.; Morin, C.; Plante, M.; Gregoire, J.; Renaud, M.C.; Sebastianelli, A.; Bachvarov, D.
Role of the polypeptide N-acetylgalactosaminyltransferase 3 in ovarian cancer progression: possible implications in abnormal mucin O-glycosylation
Oncotarget
5
544-560
2014
Homo sapiens
Gomez, H.; Rojas, R.; Patel, D.; Tabak, L.A.; Lluch, J.M.; Masgrau, L.
A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2
Org. Biomol. Chem.
12
2645-2655
2014
Homo sapiens (Q10471), Homo sapiens
Mochizuki, Y.; Ito, K.; Izumi, H.; Kohno, K.; Amano, J.
Expression of polypeptide N-acetylgalactosaminyl transferase-3 and its association with clinicopathological factors in thyroid carcinomas
Thyroid
23
1553-1560
2013
Homo sapiens (Q14435), Homo sapiens
Yu, C.; Liang, L.; Yin, Y.
Structural basis of carbohydrate transfer activity of UDP-GalNAc Polypeptide N-acetylgalactosaminyltransferase 7
Biochem. Biophys. Res. Commun.
510
266-271
2019
Homo sapiens (Q86SF2)
Shan, A.; Lu, J.; Xu, Z.; Li, X.; Xu, Y.; Li, W.; Liu, F.; Yang, F.; Sato, T.; Narimatsu, H.; Zhang, Y.
Polypeptide N-acetylgalactosaminyltransferase 18 non-catalytically regulates the ER homeostasis and O-glycosylation
Biochim. Biophys. Acta
1863
870-882
2019
Homo sapiens (Q6P9A2)
Lackman, J.J.; Goth, C.K.; Halim, A.; Vakhrushev, S.Y.; Clausen, H.; Petaejae-Repo, U.E.
Site-specific O-glycosylation of N-terminal serine residues by polypeptide GalNAc-transferase 2 modulates human delta-opioid receptor turnover at the plasma membrane
Cell. Signal.
42
184-193
2018
Homo sapiens (Q10471), Homo sapiens
Yan, X.; Lu, J.; Zou, X.; Zhang, S.; Cui, Y.; Zhou, L.; Liu, F.; Shan, A.; Lu, J.; Zheng, M.; Feng, B.; Zhang, Y.
The polypeptide N-acetylgalactosaminyltransferase 4 exhibits stage-dependent expression in colorectal cancer and affects tumorigenesis, invasion and differentiation
FEBS J.
285
3041-3055
2018
Homo sapiens (Q8N4A0), Homo sapiens
Choi, J.; Wagner, L.J.S.; Timmermans, S.B.P.E.; Malaker, S.A.; Schumann, B.; Gray, M.A.; Debets, M.F.; Takashima, M.; Gehring, J.; Bertozzi, C.R.
Engineering orthogonal polypeptide GalNAc-transferase and UDP-sugar pairs
J. Am. Chem. Soc.
141
13442-13453
2019
Homo sapiens (Q10471), Homo sapiens
Goth, C.K.; Tuhkanen, H.E.; Khan, H.; Lackman, J.J.; Wang, S.; Narimatsu, Y.; Hansen, L.H.; Overall, C.M.; Clausen, H.; Schjoldager, K.T.; Petaejae-Repo, U.E.
Site-specific O-glycosylation by polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) co-regulates beta1-adrenergic receptor N-terminal cleavage
J. Biol. Chem.
292
4714-4726
2017
Homo sapiens (Q10471)
Hintze, J.; Ye, Z.; Narimatsu, Y.; Madsen, T.D.; Joshi, H.J.; Goth, C.K.; Linstedt, A.; Bachert, C.; Mandel, U.; Bennett, E.P.; Vakhrushev, S.Y.; Schjoldager, K.T.
Probing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines
J. Biol. Chem.
293
19064-19077
2018
Homo sapiens (Q10471), Homo sapiens (Q8NCW6)
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Release 2023.1 (January 2023)
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